Comparative Immunological Studies of TwoPseudomonasEnzymes

Crystalline preparations of muconate lactonizing enzyme and muconolactone isomerase, two inducible enzymes that catalyze successive steps in the catechol branch of the β-ketoadipate pathway, were used to prepare antisera. Both enzymes were isolated from a strain ofPseudomonas putida biotype A. The antisera did not cross-react with enzymes of the same bacterial strain that catalyze the chemically analogous steps in the protocatechuate branch of the β-ketoadipate pathway, carboxymuconate lactonizing enzyme and carboxymuconolactone decarboxylase. The antisera gave heterologous cross-reactions of varying intensities with the muconate lactonizing enzymes and muconolactone isomerases ofP. putida biotype B,P. aeruginosa, P. stutzeri , and all biotypes ofP. fluorescens , but did not cross-react with the isofunctional enzymes ofP. acidovorans , ofP. multivorans , and of two bacterial species that belong to other genera. The evolutionary and taxonomic implications of the findings are discussed.